P53蛋白质R175残基替换的分子动力学研究

利用Ｐ５３蛋白核心区晶体结构作分子动力学研究发现，除了生经方面的稳定性之外，该区还具有分子动力学上的高度稳定性。在此基础上作的Ｒ１７５残基替换分子动力学研究显示，Ｐ５３蛋白质核心区１７５位点精氨酸被其他残基替换后能引起Ｐ５３蛋白质核心区Ｌ２、Ｌ３结构域间的密切联系趋于松散，下沉遥空间构象发生改变并使整个核心区结构稳定性受到破坏。这一研究从三维结构变化上，直观地解释了Ｒ１７５钱基替换造成的５３蛋白质

MOLECULAR DYNAMICS RESEARCH ON R175 RESIDUE SUBSTITUTION IN P53 PROTEIN

The molecular dynamics research of the core domain of p53 protein crystal structure shows that besides the stability in biochemistry this domain also shows a high stability in molecular mechanics. Based on this work, we substituted the residue R175 with some other amino acids and performed molecular dynamics researches separately. The results show that substitution of R175 causes a relax tendency between loop2 and 3 domains, leading to an alteration of the whole conformation of p53 core domain and ruining its stability. This research visually explains the mechanism of p53 changes in immunological and biochemical reactions, which are caused by R175 substitutions leading to the 3-D structure variations.